Cited by 868Protein Interaction Studies and Fluorescence AnalysisProtein Structure and DynamicsEnzyme Structure and Function

The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.

The lipocalin protein family: structural and sequence overview

Flower, Darren R., North, Anthony C.T., Sansom, Clare E.·2000·Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

DOI 10.1016/s0167-4838(00)00148-5

Open this paper in CoChat — free account

Abstract

Lipocalins are remarkably diverse at the sequence level yet have highly conserved structures. Most lipocalins share three characteristic conserved sequence motifs - the kernel lipocalins - while others are more divergent family members - the outlier lipocalins - typically sharing only one or two. This classification is a useful tool for analysing the family, and within these large sets are smaller groups sharing much higher levels of sequence similarity. The lipocalins are also part of a larger protein superfamily: the calycins, which includes the fatty acid binding proteins, avidins, a group of metalloproteinase inhibitors, and triabin. The superfamily is characterised by a similar structure (a repeated +1 topology beta-barrel) and by the conservation of a remarkable structural signature.

Integrity signals

Registry

Crossref · 10.1016/s0167-4838(00)00148-5

Cites

59 of 59 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

SCOP: A structural classification of proteins database for the investigation of sequences and structures
Murzin, A. G., Brenner, S. E., Hubbard, T., & Chothia, C. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80134-2 · Cited by 6,445
The lipocalin protein family: structure and function
FLOWER, D. R. (1996) · Biochemical Journal · doi:10.1042/bj3180001 · Cited by 1,679
Self-citation
The PROSITE database, its status in 1999
Hofmann, K., Bücher, P., Falquet, L., & Bairoch, A. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.1.215 · Cited by 1,092
[5] Avidin and streptavidin
Green, N. M. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)84259-j · Cited by 1,020
Bovine β-lactoglobulin at 1.8 Å resolution — still an enigmatic lipocalin
Brownlow, S., Morais-Cabral, J. H., Cooper, R. A., Flower, D. R., Yewdall, S. J., Polikarpov, I., North, A. C. T., & Sawyer, L. (1997) · Structure · doi:10.1016/s0969-2126(97)00205-0 · Cited by 714
Self-citation
Lipid-Binding Proteins: A Family of Fatty Acid and Retinoid Transport Proteins
Banaszak, L. J., Winter, N. S., Xu, Z., Bernlohr, D., Cowan, S. W., & Jones, A. T. (1994) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60639-7 · Cited by 483
1.4 .ANG. Structure of Photoactive Yellow Protein, a Cytosolic Photoreceptor: Unusual Fold, Active Site, and Chromophore
Borgstahl, G. E. O., Williams, D. R., & Getzoff, E. D. (1995) · Biochemistry · doi:10.1021/bi00019a004 · Cited by 438
Many of the Immunoglobulin Superfamily Domains in Cell Adhesion Molecules and Surface Receptors Belong to a New Structural Set Which is close to That Containing Variable Domains
Harpaz, Y., & Chothia, C. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1312 · Cited by 435
Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography
Böcskei, Z., Groom, C. R., Flower, D. R., Wright, C. E., Phillips, S. E. V., Cavaggioni, A., Findlay, J. B. C., & North, A. C. T. (1992) · Nature · doi:10.1038/360186a0 · Cited by 361
Self-citation
Structure and sequence relationships in the lipocalins and related proteins
Flower, D. R., North, A. C. T., & Attwood, T. K. (1993) · Protein Science · doi:10.1002/pro.5560020507 · Cited by 342
Self-citation

Show all 59 references

Sorted by citations

Items 801–867 of 867

Lipocalina bovina e o seu papel na resistência ao carrapato: quantificação em líquidos corporais de raças bovinas com fenótipos contrastantes de infestações com o carrapato Rhipicephalus microplus
de Carvalho, J. A. (2017) · doi:10.11606/d.17.2017.tde-06062017-161955
Determining the Role of Tubulointerstitial Nephritis Antigen-Like 1 in Renal Ischemic Reperfusion Injury
Pang, P. D. (2018) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)
Prediction of Plant Lipocalin Genes based on Convolutional Neural Networks
Hu, S., Liao, Z., & Jia, H. (2019) · International Conference on Artificial Intelligence and Computer Science (AICS) · doi:10.1145/3349341.3349451
α2u-Globulin Nephropathy
Lehman‐McKeeman, L. D. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.95648-4
Diagnostica dell'insufficienza renale acuta e biomarkers di danno renale
Lentini, P. L. M., de Cal, M., Zanoli, L., Granata, A. R. M., & Dell’Aquila, R. (2016) · Giornale di Clinica Nefrologica e Dialisi · doi:10.33393/gcnd.2016.763
STUDY OF SERUM NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN CONCENTERATIONS AS A MARKER OF RENAL FUNCTION IN CHRONIC KIDNEY DISEASE PATIENTS
Kaushik, G. G., Maheshwari, S., & Sharma, A. (2021) · GLOBAL JOURNAL FOR RESEARCH ANALYSIS · doi:10.36106/gjra/8514421
Computational approaches to discover novel enzymes for fragrance and flavour
Durairaj, J. (2021) · doi:10.18174/551031
THE ROLE OF NEW BIOMARKERS IN ACUTE KIDNEY INJURY DETECTING IN CRITICAL CONDITION PATIENTS
Sharipova, V. K., Berdiev, N. F., Lutfullaev, O. K. L., & Mikhliev, A. N. (2021) · The Bulletin of Emergency Medicine · doi:10.54185/tbem/vol14_iss3/a10
Molecular Dynamical Investigation of a YodA Protein Signifies Zinc Ion-Residues Interactions
Chaturvedi, N., & Pandey, P. N. (2020) · JOURNAL OF INTERNATIONAL ACADEMY OF PHYSICAL SCIENCES
Approche bioinformatique et fonctionnelle pour la caractérisation de protéines sécrétées chez les Trypanosomatidés : implication dans la biologie et la virulence du parasite
Corrales, R. M. (2009) · OpenGrey (Institut de l'Information Scientifique et Technique)
An Examination of Bone Loss During Space Travel with Differential Gene Expression Analysis
Vo, C. (2021) · doi:10.31979/etd.an9m-wtkd
Recognition Units
(2008) · Springer eBooks · doi:10.1007/978-1-4020-9003-5_5
Introduction
Pevsner, J. (2009) · doi:10.1002/9780470451496.ch1
Estudio sobre la interacción entre la β-Lactoglobulina y la β-Galactosidasa de Kluyveromyces lactis y el papel que juegan los aminoácidos de las proteínas en la interacción y el efecto activador sobre la enzima
Moral-Ramírez, E. D. (2012) · doi:10.24275/uami.f4752g95x
Peer Review #1 of "Structure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants (v0.1)"
(2016) · PeerJ · doi:10.7287/peerj.1933v0.1/reviews/1
Complement Protein C8
Sodetz, J. M., & Lebioda, L. (2005) · CRC Press eBooks · doi:10.1201/9780849350368.ch10
Peer Review #1 of "Structure and stability of recombinant bovine odorant-binding protein: III. Peculiarities of the wild type bOBP unfolding in crowded milieu (v0.2)"
(2016) · PeerJ · doi:10.7287/peerj.1642v0.2/reviews/1
Peer Review #2 of "Structure and stability of recombinant bovine odorant-binding protein: III. Peculiarities of the wild type bOBP unfolding in crowded milieu (v0.2)"
(2016) · PeerJ · doi:10.7287/peerj.1642v0.2/reviews/2
Peer Review #1 of "Structure and stability of recombinant bovine odorant-binding protein: III. Peculiarities of the wild type bOBP unfolding in crowded milieu (v0.1)"
(2016) · PeerJ · doi:10.7287/peerj.1642v0.1/reviews/1
Peer Review #2 of "Structure and stability of recombinant bovine odorant-binding protein: III. Peculiarities of the wild type bOBP unfolding in crowded milieu (v0.1)"
(2016) · PeerJ · doi:10.7287/peerj.1642v0.1/reviews/2
Descrição extensiva dos sialomas de Rhodnius neglectus e Triatoma dimidiata, vetores da doença de Chagas
Santiago, P. B. (2016) · doi:10.26512/2016.t.24792
Peer Review #3 of "Structure and stability of recombinant bovine odorant-binding protein: III. Peculiarities of the wild type bOBP unfolding in crowded milieu (v0.1)"
(2016) · PeerJ · doi:10.7287/peerj.1642v0.1/reviews/3
Peer Review #1 of " Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms (v0.1)"
(2016) · PeerJ · doi:10.7287/peerj.1574v0.1/reviews/1
Peer Review #1 of " Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms (v0.2)"
(2016) · PeerJ · doi:10.7287/peerj.1574v0.2/reviews/1
Peer Review #3 of "Structure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants (v0.2)"
(2016) · PeerJ · doi:10.7287/peerj.1933v0.2/reviews/3
Peer Review #2 of "Structure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants (v0.2)"
(2016) · PeerJ · doi:10.7287/peerj.1933v0.2/reviews/2
Peer Review #2 of " Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms (v0.1)"
(2016) · PeerJ · doi:10.7287/peerj.1574v0.1/reviews/2
G-domain prediction across the diversity of G protein families
Hiral, H. (2020) · doi:10.26226/morressier.5ebd45acffea6f735881b17f
Peer Review #2 of "Structure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants (v0.1)"
(2016) · PeerJ · doi:10.7287/peerj.1933v0.1/reviews/2
IDENTIFICATION OF PUTATIVE MUP DURING ESTRUS PERIOD IN FEMALE RAJAPALAYAM BREED DOG BY MALDI-TOF ANALYSIS
RAJAGOPAL, T., DHIVYA, A., GAYATHRI, T. R., MURUGANANTHAM, N., Subbiah, S., Ponmanickam, P., MUNIASAMY, S., & Archunan, G. (2022) · Asian Journal of Microbiology Biotechnology and Environmental Sciences · doi:10.53550/ajmbes.2022.v24i04.027
Sensors Based on Peptides and Proteins as Recognition Units
Demchenko, A. P. (2023) · Springer eBooks · doi:10.1007/978-3-031-19089-6_4
Value addition to acid whey from greek yogurt processing with millets (kodo and proso) for development of nutritious food products
Malik, S. (2022) · doi:10.32469/10355/94286
Data from Inhibition of Lipocalin 2 Impairs Breast Tumorigenesis and Metastasis
Leng, X., Ding, T., Lin, H., Wang, Y., Hu, L., Hu, J., Feig, B. W., Zhang, W., Pusztai, L., Symmans, W. F., et al. (2023) · doi:10.1158/0008-5472.c.6500246
Identification of hub genes and biological process analysis of otosclerosis patients based on WGCNA analysisPreprint
Wang, W., Zhang, D., Lei, M., Wang, Y., Zeng, P., Zou, C., Hong, Y., & Cai, C. (2023) · Research Square · doi:10.21203/rs.3.rs-2781561/v1
Tributyltin-binding protein type 1 (fish acid glycoprotein) is a potential gatekeeper of ethinylestradiol action in fish
Hakata, H., Takai, Y., Lee, J. M., Kusakabe, T., Satone, H., Shimasaki, Y., & Oshima, Y. (2023) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2023.109660
Clonagem, expressão e purificação de um domínio hipotético de ligação a ácidos graxos em Leishmania amazonensis para ensaios de biologia estrutural
Athayde, L. F. A. (2023) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.46.2023.tde-11122023-162533
Identification, Tissue Expression, and Response to Various Fatty Acid Inductions of the Fabp Gene Family in Grass Carp (Ctenopharyngodon Idella)Preprint
Zhang, Y., Fan, H., Gao, K., Zhang, S., Lu, R., Cao, X., Xu, X., & Liu, J. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4858566
α2u-Globulin Nephropathy
Lehman‐McKeeman, L. D. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.00125-x
Artificial olfactory systems: Mimicking the sense of smell
Brito, N. F. (2025) · Comprehensive analytical chemistry · doi:10.1016/bs.coac.2025.04.001 · Cited by 1
Discovery of rim region between core and surface of proteins
Bandyopadhyay, A. K., Banerjee, S., & Das, S. (2024) · doi:10.52756/lbsopf.2024.e03.003
Soluble carrier proteins: from chemical communication to developmental biology and artificial sensing
Zhu, J., Zaremska, V., Knoll, W., & Pelosi, P. (2025) · Chemical Senses · doi:10.1093/chemse/bjaf025
Plasma concentrations of the inflammatory adipokine lipocalin-2 are not affected by chronic alcohol exposure in rats or acute alcohol administration in people with alcohol use disorder
Richardson, R. S., Farokhnia, M., Vendruscolo, L. F., & Leggio, L. (2025) · The American Journal of Drug and Alcohol Abuse · doi:10.1080/00952990.2025.2582563
Odorant-Receptor Interaction
Su, X., Matsunami, H., & Zhuang, H. (2014) · Springer eBooks · doi:10.1007/978-94-017-8613-3_4
Roles of the mitogen-induced proteins, mitogen regulated protein/proliferin and 24p3/uterocalin, during mouse development
Lepont, P. (2002) · doi:10.31274/rtd-180813-11434
Designing High-Affinity Progesterone Binders: Pocket Analysis and Scaffold SelectionPreprint
Pourhassan‐Moghaddam, M., Cornell, B. A., & Valenzuela, S. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.12.704737
Research Progress of Lipocalin-2 in Tumors
刘, 昊. (2026) · Advances in Clinical Medicine · doi:10.12677/acm.2026.163871
Immunological functional studies of a putative lipocalin member LcApoM_AGPRP in large yellow croaker (Larimichthys crocea)
Huang, R., Yan, C., Lv, Y., Jin, Y., & Zhang, D. (2026) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2026.111274
Identification and characterisation of the ornate spiny lobster Panulirus ornatus crustacyanins and their role in colourationPreprint
Yoon, J., Banks, T. M., Kelly, T., Smith, G., Fitzgibbon, Q. P., & Ventura, T. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.6482319
Etude des relations entre la structure des molécules odorantes et leurs équilibres rétention-libération entre phase vapeur et gels laitiers
Merabtine, Y. (2010) · theses.fr (ABES) · doi:10.70675/905f8b5ez6762z40e9zb85czdbf24e71ea6a
Caractérisation de l'interaction protéine-ligand sous l'effet de la pression isisatique ou dynamique : application à l’inclusion de composés hydrophobes dans des nanostructures élaborées à partir de protéines du lait.
Blayo, C. (2012) · doi:10.70675/5c215eaezf26fz44efza090zedcc28d823de
Structure and Rheology of complex liquids and gels containing polysaccharides and proteins
Nguyen, B. T. (2014) · doi:10.70675/e363d209z4b20z4237z9411z1c744ff88cd9
Rôle de la Sélénoprotéine T dans le remodelage cardiaque post-infarctus et le développement de l'insuffisance cardiaque.
Boukhalfa, I. (2017) · theses.fr (ABES) · doi:10.70675/f17724cbz825ez4a0az9c31z0b10d6d5f706
L'intrigant couplage radicalaire stéréosélectif médié par la protéine dirigeante AtDIR6
Modolo, C. (2017) · theses.fr (ABES) · doi:10.70675/1411461az310fz42e6z8258zecd3cf6cd123
Stratégies de stimulation du transport axonal endogène du Bdnf comme piste thérapeutique dans le syndrome de Rett
Ehinger, Y. (2018) · theses.fr (ABES) · doi:10.70675/b9d2d0e4z8d00z4bcfza57bz31ca5ed1866c
Role of odorant-binding proteins in Drosophila melanogaster chemosensory perception
Rihani, K. (2019) · theses.fr (ABES) · doi:10.70675/a9a9ebf6z8bf0z4537zaae8zdbdc08eccb5a
Understanding the relationship between antibacterial activity and iron-restriction mechanisms in egg-white
Julien, L. A. (2020) · theses.fr (ABES) · doi:10.70675/87fe6365z7ce8z43f8zbecbzf1b4ca746558
Implication of an odorant-binding protein in precopulatory behaviour and interaction with the bacterial microbiota
Aruçi, E. (2023) · theses.fr (ABES) · doi:10.70675/87239574zb878z46fazb9c4z46257efd2a21
A conserved sequence insert of fibrillins is involved in plastoglobule association and lipid binding
Shivaiah, K., Kithan-Lundquist, R., Kaneshiro, A. K., Boren, D. M., Susanto, F. A., Herrera-Tequia, A., Vermaas, J. V., & Lundquist, P. K. (2026) · Plant and Cell Physiology · doi:10.1093/pcp/pcag047 · Cited by 4
Hippocampal Lipocalin-2 in T2DM Associated Neurodegeneration: A Therapeutic Perspective
Panigrahy, B., Mukherjee, A., & Singh, S. (2026) · Neurochemical Research · doi:10.1007/s11064-026-04765-z
Colchicine alleviates severe acute pancreatitis in rats by inhibiting acinar cell ferroptosis via LCN2/MAPK/ERK signaling axis
Yang, L., Zheng, X., Zhang, Y., Li, Y., Li, L., & Liu, F. (2026) · European Journal of Histochemistry · doi:10.4081/ejh.2026.4557
A lipocalin and a Hedgehog-related protein are partners in the Caenorhabditis elegans precuticle apical extracellular matrix
Serra, N. D., Chen, J., Birnbaum, S. K., Aviles, S. G., & Sundaram, M. V. (2026) · Genetics · doi:10.1093/genetics/iyag218
Apolipoprotein D3 is required for long‐chain cuticular hydrocarbon accumulation and water retention in Acyrthosiphon pisum
Wu, B., Yang, X., Mobarak, S. H., Li, L., Zhang, Z., Basit, A., & Qiao, J. (2026) · Pest Management Science · doi:10.1002/ps.71309
Production and characterization of diagnostic-grade recombinant allergens: from expression platform selection to clinical application
Dvareckienė, J. (2026) · doi:10.15388/vu.thesis.962
A lipocalin-like cyclase drives cyclopenta[b]fluorene core assembly in antitumor ascomylactam biosynthesis
Yang, W., Chen, Y., Liu, L., Qi, S.-H., She, Z., & Li, H. (2026) · Chinese Chemical Letters · doi:10.1016/j.cclet.2026.113559
BindingDB Entry 50021299: Recent Advances on Small-Molecule Inhibitors of Lipocalin-like Proteins.
BindingDB (2025) · UC San Diego · doi:10.7270/q2x3533h
Wrapping mechanism of β-lactoglobulin around SDS micelles characterized by time-resolved vacuum-ultraviolet circular dichroism and molecular dynamics simulation
Hashimoto, S., & Matsuo, K. (2026) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2026.129061
The roles of Lcn2 in the inflammatory lung and liver
Liu, Y. (2007) · doi:10.31274/rtd-180813-4555

Authors: Flower, D. R., North, A. C. T., & Sansom, C. E.
Affiliations: Jenner Institute (GB)
University of Leeds (GB)
University of London (GB)
Corresponding author: Flower, Darren R.
ORCID: Flower, Darren R.
Venue: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Publisher: Elsevier BV
Published: 2000-10
Volume: 1482
Issue: 1-2
Pages: 9-24
ISSN: 0167-4838 (ISSN-L)
DOI: 10.1016/s0167-4838(00)00148-5
OpenAlex: W2038438679
Cited by: 868
References: 59
Citations by year: 2026: 18 · 2025: 26 · 2024: 25 · 2023: 27 · 2022: 29 · 2021: 33 · 2020: 37 · 2019: 27 · 2018: 29 · 2017: 35 · 2016: 46 · 2015: 39 · 2014: 51 · 2013: 37 · 2012: 60
FWCI: 1.34
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: lipocalin, protein superfamilies, conserved motifs, fatty acid binding protein, avidin, metalloproteinase inhibitors, protein structure conservation
MeSH terms: Fatty Acid-Binding Protein 7, Amino Acid Sequence, Animals, Carrier Proteins, Humans, Lactoglobulins, Models, Molecular, Molecular Sequence Data, Neoplasm Proteins, Protein Conformation, Sequence Homology, Amino Acid, Insect Proteins, Tumor Suppressor Proteins, Fatty Acid-Binding Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

The lipocalin protein family: structural and sequence overview

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks